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Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum
Author(s) -
Lu ChungLing,
Ortmeier Steven,
Brudvig Jon,
Moretti Tamara,
Cain Jacob,
Boyadjiev Simeon A.,
Weimer Jill M.,
Kim Jinoh
Publication year - 2022
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12826
Subject(s) - endoplasmic reticulum , biology , secretion , phenotype , microbiology and biotechnology , procollagen peptidase , copii , secretory protein , mutant , secretory pathway , fibronectin , genetics , gene , golgi apparatus , extracellular matrix , biochemistry
Abstract SEC24 is mainly involved in cargo sorting during COPII vesicle assembly. There are four SEC24 paralogs (A–D) in vertebrates, which are classified into two subgroups (SEC24A/B and SEC24C/D). Pathological mutations in SEC24D cause osteogenesis imperfecta with craniofacial dysplasia in humans. sec24d mutant fish also recapitulate the phenotypes. Consistent with the skeletal phenotypes, the secretion of collagen was severely defective in mutant fish, emphasizing the importance of SEC24D in collagen secretion. However, SEC24D patient‐derived fibroblasts show only a mild secretion phenotype, suggesting tissue‐specificity in the secretion process. Using Sec24d KO mice and cultured cells, we show that SEC24A and SEC24B also contribute to endoplasmic reticulum (ER) export of procollagen. In contrast, fibronectin 1 requires either SEC24C or SEC24D for ER export. On the basis of our results, we propose that procollagen interacts with multiple SEC24 paralogs for efficient export from the ER, and that this is the basis for tissue‐specific phenotypes resulting from SEC24 paralog deficiency.